![]()
|
|
||||||||
J. Biol. Chem., Vol. 280, Issue 7, 6072-6079, February 18, 2005
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||


From the
Department of Neurology¶, University of Alabama at Birmingham, Birmingham, Alabama, 35294, ¶Structural Motility, UMR144, Institut Curie Centre National de la Recherche Scientifique, 26 Rue d'Ulm, 75248 Paris, France, and the ||Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104
Processivity in myosin V is mediated through the mechanical strain that results when both heads bind strongly to an actin filament, and this strain regulates the timing of ADP release. However, what is not known is which steps that lead to ADP release are affected by this mechanical strain. Answering this question will require determining which of the several potential pathways myosin V takes in the process of ADP release and how actin influences the kinetics of these pathways. We have addressed this issue by examining how magnesium regulates the kinetics of ADP release from myosin V and actomyosin V. Our data support a model in which actin accelerates the release of ADP from myosin V by reducing the magnesium affinity of a myosin V-MgADP intermediate. This is likely a consequence of the structural changes that actin induces in myosin to release phosphate. This effect on magnesium affinity provides a plausible explanation for how mechanical strain can alter this actin-induced acceleration. For actomyosin V, magnesium release follows phosphate release and precedes ADP release. Increasing magnesium concentration to within the physiological range would thus slow both the ATPase activity and the velocity of movement of this motor.
Received for publication, November 10, 2004 , and in revised form, November 30, 2004.
* This work was supported by Grants AR048565 (to S. S. R.) and AR35661 (to H. L. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Neurology, University of Alabama at Birmingham, FOT 1020, 1530 3rd Ave. South, Birmingham, AL 35294. E-mail: stevensr{at}uab.edu.
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
M. H. Taft, F. K. Hartmann, A. Rump, H. Keller, I. Chizhov, D. J. Manstein, and G. Tsiavaliaris Dictyostelium Myosin-5b Is a Conditional Processive Motor J. Biol. Chem., October 3, 2008; 283(40): 26902 - 26910. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. R. Hodges, E. B. Krementsova, and K. M. Trybus Engineering the Processive Run Length of Myosin V J. Biol. Chem., September 14, 2007; 282(37): 27192 - 27197. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. Iorga, N. Adamek, and M. A. Geeves The Slow Skeletal Muscle Isoform of Myosin Shows Kinetic Features Common to Smooth and Non-muscle Myosins J. Biol. Chem., February 9, 2007; 282(6): 3559 - 3570. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. C. M. Gebhardt, A. E.-M. Clemen, J. Jaud, and M. Rief From the Cover: Myosin-V is a mechanical ratchet PNAS, June 6, 2006; 103(23): 8680 - 8685. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. R. Guydosh and S. M. Block Backsteps induced by nucleotide analogs suggest the front head of kinesin is gated by strain PNAS, May 23, 2006; 103(21): 8054 - 8059. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Sun, J. L. Oakes, S. K. Ananthanarayanan, K. H. Hawley, R. Y. Tsien, S. R. Adams, and C. M. Yengo Dynamics of the Upper 50-kDa Domain of Myosin V Examined with Fluorescence Resonance Energy Transfer J. Biol. Chem., March 3, 2006; 281(9): 5711 - 5717. [Abstract] [Full Text] [PDF] |
||||
![]() |
U. Durrwang, S. Fujita-Becker, M. Erent, F. J. Kull, G. Tsiavaliaris, M. A. Geeves, and D. J. Manstein Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis J. Cell Sci., February 1, 2006; 119(3): 550 - 558. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. O. Olivares and E. M. De La Cruz Holding the reins on Myosin V PNAS, September 27, 2005; 102(39): 13719 - 13720. [Full Text] [PDF] |
||||
![]() |
T. J. Purcell, H. L. Sweeney, and J. A. Spudich From the Cover: A force-dependent state controls the coordination of processive myosin V PNAS, September 27, 2005; 102(39): 13873 - 13878. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |